title: Methylation of elongation factor 1 alpha from the fungus Mucor.
abstract: A basic protein from the dimorphic fungus Mucor racemosus, found to be highly methylated, is shown to be protein synthesis elongation factor 1 alpha. This protein is the most abundant protein in hyphal cells but is less abundant in yeast cells. It is post-translationally methylated with the formation of mono-, di-, and trimethyllysine at as many as 16 sites. Nearly 20% of the 44 lysine residues of elongation factor 1 alpha from mycelia are modified while those from sporangiospores are virtually unmethylated.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D005656:Fungal Proteins / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D046911:Macromolecular Substances; D008745:Methylation; D009024:Morphogenesis; D009089:Mucor / Q000378:metabolism* / Q000502:physiology; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D000596:Amino Acids; D005656:Fungal Proteins; D046911:Macromolecular Substances; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D008239:Lysine